4f3z
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f3z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f3z RCSB], [http://www.ebi.ac.uk/pdbsum/4f3z PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f3z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f3z RCSB], [http://www.ebi.ac.uk/pdbsum/4f3z PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/Q8QT89_9INFA Q8QT89_9INFA]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324][SAAS:SAAS00145386] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 00:47, 25 December 2014
Crystal structure of a swine H1N2 influenza virus hemagglutinin
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